P34038 (KPYK_LACDE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pyruvate kinase
Short name=PK
EC=2.7.1.40

Gene names

Name:

pyk

Organism

Lactobacillus delbrueckii subsp. bulgaricus

Taxonomic identifier

1585 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Lactobacillales › Lactobacillaceae › Lactobacillus › Lactobacillus delbrueckii

Protein attributes

Sequence length	589 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + pyruvate = ADP + phosphoenolpyruvate.
Cofactor	Magnesium. Potassium.
Enzyme regulation	Strongly activated by glucose-6-phosphate, ribose-5-phosphate and fructose-6-phosphate. Weak activator AMP and weak inhibitor fructose-1,6-bisphosphate can act as strong inhibitors in the presence of strong activators.
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
Subunit structure	Homotetramer.
Sequence similarities	Belongs to the pyruvate kinase family. In the C-terminal section; belongs to the PEP-utilizing enzyme family.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding Potassium Pyruvate
Molecular function	Kinase Transferase
Technical term	Allosteric enzyme Direct protein sequencing
Gene Ontology (GO)
Biological_process	glycolysis Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: InterPro potassium ion binding Inferred from electronic annotation. Source: InterPro pyruvate kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 589	589	Pyruvate kinase		PRO_0000112076
Sites
	Metal binding	34	1	Potassium By similarity
	Metal binding	36	1	Potassium By similarity
	Metal binding	66	1	Potassium By similarity
	Metal binding	67	1	Potassium; via carbonyl oxygen By similarity
	Metal binding	223	1	Magnesium By similarity
	Metal binding	247	1	Magnesium By similarity
	Binding site	32	1	Substrate By similarity
	Binding site	246	1	Substrate; via amide nitrogen By similarity
	Binding site	247	1	Substrate; via amide nitrogen By similarity
	Binding site	279	1	Substrate By similarity
	Site	221	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	P34038 [UniParc]. Last modified February 1, 1996. Version 3. Checksum: 2BA3D3CF7AE290F1	FASTA	589	62,920
	10 20 30 40 50 60 MKKTKIVSTL GPASDDIETI TKLAEAGANV FRFNFSHGNH EEHLARMNMV REVEKKTGKL 70 80 90 100 110 120 LGIALDTKGA EIRTTDQEGG KFTINTGDEI RVSMDATKAG NKDMIHVTYP GLFDDTHVGG 130 140 150 160 170 180 TVLIDDGAVG LTIKAKDEEK RELVCEAQNT GVIGSKKGVN APGVEIRLPG ITEKDTDDIR 190 200 210 220 230 240 FGLKHGINFI FASFVRKAQD VLDIRALCEE ANASYVKIFP KIESQEGIDN IDEILQVSDG 250 260 270 280 290 300 LMVARGDMGV EIPFINVPFV QKTLIKKCNA LGKPVITATQ MLDSMQENPR PTRAEVTDVA 310 320 330 340 350 360 NAVLDGTDAT MLSGESANGL YPVQSVQAMH DIDVRTEKEL DTRNTLALQR FEEYKGSNVT 370 380 390 400 410 420 EAIGESVVRT AQELGVKTII AATSSGYTAR MISKYRPDAT IVALTFDEKI QHSLGIVWGV 430 440 450 460 470 480 EPVLAKKPSN TDEMFEEAAR VAKEHGFVKD GDLVIIVAGV PFGQSGTTNL MKLQIIGNQL 490 500 510 520 530 540 AQGLGVGTGS VIGKAVVANS AEEANAKVHE GDILVAKTTD KDYMPAIKKA SGMIVEASGL 550 560 570 580 TSHAAVVGVS LGIPVVVGVA DATSKIADGS TLTVDARRGA IYQGEVSNL

References

[1]	"The genes for phosphofructokinase and pyruvate kinase of Lactobacillus delbrueckii subsp. bulgaricus constitute an operon." Branny P., de la Torre F., Garel J.R. J. Bacteriol. 178:4727-4730(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Cloning, sequencing, and expression in Escherichia coli of the gene coding for phosphofructokinase in Lactobacillus bulgaricus." Branny P., de la Torre F., Garel J.R. J. Bacteriol. 175:5344-5349(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-60.
[3]	"Pyruvate kinase from Lactobacillus bulgaricus: possible regulation by competition between strong and weak effectors." le Bras G., Garel J.R. Biochimie 75:797-802(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-40, CHARACTERIZATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X71403 Genomic DNA. Translation: CAA50527.1.
PIR	B48663. S35929.
3D structure databases
ProteinModelPortal	P34038.
SMR	P34038. Positions 1-589.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00109; UER00188.
Family and domain databases
Gene3D	2.40.33.10. 1 hit. 3.20.20.60. 2 hits. 3.40.1380.20. 1 hit.
InterPro	IPR008279. PEP-util_enz_mobile_dom. IPR001697. Pyr_Knase. IPR015813. Pyrv/PenolPyrv_Kinase-like_dom. IPR011037. Pyrv_Knase-like_insert_dom. IPR015794. Pyrv_Knase_a/b. IPR015793. Pyrv_Knase_brl. IPR015795. Pyrv_Knase_C. IPR015806. Pyrv_Knase_insert_dom. [Graphical view]
PANTHER	PTHR11817. PTHR11817. 1 hit.
Pfam	PF00391. PEP-utilizers. 1 hit. PF00224. PK. 1 hit. PF02887. PK_C. 1 hit. [Graphical view]
PRINTS	PR01050. PYRUVTKNASE.
SUPFAM	SSF50800. PK_B_barrel_like. 1 hit. SSF52935. Pyruvate_kinase. 1 hit. SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
TIGRFAMs	TIGR01064. pyruv_kin. 1 hit.
PROSITE	PS00110. PYRUVATE_KINASE. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

KPYK_LACDE

Accession

Primary (citable) accession number: P34038

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1996
Last modified:	May 29, 2013
This is version 90 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program